Histone acetyltransferase

histone acetylationhistone acetyltransferasesHAT histone acetyltransferases (HATs)HATshistone acetyl transferasehistone acetyl transferaseshistone acetyl transferases (HAT)Histone acetylasehistone acetylases
Histone acetyltransferases (HATs) are enzymes that acetylate conserved lysine amino acids on histone proteins by transferring an acetyl group from acetyl-CoA to form ε-N-acetyllysine.wikipedia
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Histone acetylation and deacetylation

histone acetylationAcetylationhistone deacetylation
Type A HATs are located in the nucleus and are involved in the regulation of gene expression through acetylation of nucleosomal histones in the context of chromatin.
These reactions are typically catalysed by enzymes with "histone acetyltransferase" (HAT) or "histone deacetylase" (HDAC) activity.

Transcription factor

transcription factorsgene transcription factortranscriptional factors
When it was first discovered, it was thought that acetylation of lysine neutralizes the positive charge normally present, thus reducing affinity between histone and (negatively charged) DNA, which renders DNA more accessible to transcription factors.
Other proteins such as coactivators, chromatin remodelers, histone acetyltransferases, histone deacetylases, kinases, and methylases are also essential to gene regulation, but lack DNA-binding domains, and therefore are not TFs.

Histone deacetylase

HDAChistone deacetylasesHDACs
The acetyl groups added by type B HATs to the histones are removed by HDACs once they enter the nucleus and are incorporated into chromatin.
Its action is opposite to that of histone acetyltransferase.

KAT5

HTATIPTip60Histone acetyltransferase KAT5
The MYST family of HATs is named after its four founding members MOZ, Ybf2 (Sas3), Sas2, and Tip60.
The protein encoded by this gene belongs to the MYST family of histone acetyl transferases (HATs) and was originally isolated as an HIV-1 TAT-interactive protein.

P300-CBP coactivator family

p300p300/CBPCBP/p300
Gcn5, p300/CBP, and TAF II 250 are some examples of type A HATs that cooperate with activators to enhance transcription.
In addition p300 and CBP each contain a protein or histone acetyltransferase (PAT/HAT) domain and a bromodomain that binds acetylated lysines and a PHD finger motif with unknown function.

ELP3

The Gcn5-related N-acetyltransferase (GNAT) family includes Gcn5, PCAF, Hat1, Elp3, Hpa2, Hpa3, ATF-2, and Nut1.
ELP3 is the catalytic histone acetyltransferase subunit of the RNA polymerase II elongator complex, which is a component of the RNA polymerase II (Pol II) holoenzyme and is involved in transcriptional elongation.

Histone H3

H3histone 3H3.3
These HATs are generally characterized by the presence of a bromodomain, and they are found to acetylate lysine residues on histones H2B, H3, and H4.
Acetylation of histone H3 at several lysine positions in the histone tail is performed by histone acetyltransferase enzymes (HATs).

Activating transcription factor 2

ATF2ATFATF-2
The Gcn5-related N-acetyltransferase (GNAT) family includes Gcn5, PCAF, Hat1, Elp3, Hpa2, Hpa3, ATF-2, and Nut1.
The protein is also a histone acetyltransferase (HAT) that specifically acetylates histones H2B and H4 in vitro; thus, it may represent a class of sequence-specific factors that activate transcription by direct effects on chromatin components.

Nuclear receptor coactivator 1

NCOA1SRC-1COA1
Three important nuclear receptor coactivators that display HAT activity are SRC-1, ACTR, and TIF-2.
The nuclear receptor coactivator 1 is a transcriptional coregulatory protein that contains several nuclear receptor interacting domains and an intrinsic histone acetyltransferase activity.

Acetylation

acetylateddeacetylationN-terminal acetylation
When it was first discovered, it was thought that acetylation of lysine neutralizes the positive charge normally present, thus reducing affinity between histone and (negatively charged) DNA, which renders DNA more accessible to transcription factors. Histone acetyltransferases (HATs) are enzymes that acetylate conserved lysine amino acids on histone proteins by transferring an acetyl group from acetyl-CoA to form ε-N-acetyllysine.
Typically, these reactions are catalyzed by enzymes with histone acetyltransferase (HAT) or histone deacetylase (HDAC) activity, although HATs and HDACs can modify the acetylation status of non-histone proteins as well.

HAT1

Hat1 is one of the few known examples of a type B HAT.
The protein encoded by this gene is a type B histone acetyltransferase (HAT) that is involved in the rapid acetylation of newly synthesized cytoplasmic histones, which are, in turn, imported into the nucleus for de novo deposition onto nascent DNA chains.

Nuclear receptor coactivator 3

NCOA3ACTRSRC3
Three important nuclear receptor coactivators that display HAT activity are SRC-1, ACTR, and TIF-2.
NCOA3 is a transcriptional coactivator protein that contains several nuclear receptor interacting domains and an intrinsic histone acetyltransferase activity.

Nuclear receptor coactivator 2

NCOA2GRIP-1SRC2
Three important nuclear receptor coactivators that display HAT activity are SRC-1, ACTR, and TIF-2.
NCoA-2 is a transcriptional coregulatory protein that contains several nuclear receptor interacting domains and an intrinsic histone acetyltransferase activity.

Bromodomain

Bromodomain and Extra-Terminal motif (BET) protein familyBromodomain and Extra-Terminal motif (BET) proteinsBromodomain-containing protein
Research has emerged, since, to show that lysine acetylation and other posttranslational modifications of histones generate binding sites for specific protein–protein interaction domains, such as the acetyllysine-binding bromodomain.
Histone acetyltransferases, including EP300 and PCAF, have bromodomains in addition to acetyl-transferase domains.

Myc

c-MyccMycc-Myb
PCAF has also been observed to acetylate c-MYC, GATA-2, retinoblastoma (Rb), Ku70, and E1A adenovirus protein.
In addition to its role as a classical transcription factor, N-myc may recruit histone acetyltransferases (HATs).

Histone

histoneshistone modificationhistone modifications
Histone acetyltransferases (HATs) are enzymes that acetylate conserved lysine amino acids on histone proteins by transferring an acetyl group from acetyl-CoA to form ε-N-acetyllysine.

Zinc finger

zinc-fingerzinc finger proteinzinc fingers
These HATs are typically characterized by the presence of zinc fingers and chromodomains, and they are found to acetylate lysine residues on histones H2A, H3, and H4.

Proliferating cell nuclear antigen

PCNA
p300/CBP have also been observed to acetylate β-catenin, RIP140, PCNA, the DNA metabolic enzymes flap endonuclease-1, thymine DNA glycosylase, and Werner syndrome DNA helicase, STAT6, Runx1 (AML1), UBF, Beta2/NeuroD, CREB, c-Jun, C/EBPβ, NF-E2, SREBP, IRF2, Sp3, YY1, KLF13, EVI1, BCL6, HNF-4, ER81 and FOXO4 (AFX).

Chromatin remodeling

chromatin remodelerschromatin remodellingremodeled
Controlling the chromatin remodeling process within cancer cells may provide a novel drug target for cancer research.

Histone code

H3K9mono and di-methylationtable below
These combinations of different covalent modifications on the N-terminal tails of histones have been referred to as the histone code, and it is thought that this code may be heritable and preserved in the next cell generation.

Histone methyltransferase

histone-lysine N-methyltransferaseHistone Lysine MethyltransferasesHistone methyltransferase (HMT)

Enzyme

enzymologyenzymesenzymatic
Histone acetyltransferases (HATs) are enzymes that acetylate conserved lysine amino acids on histone proteins by transferring an acetyl group from acetyl-CoA to form ε-N-acetyllysine.

Lysine

Lyslysine degradationL-lysine
Histone acetyltransferases (HATs) are enzymes that acetylate conserved lysine amino acids on histone proteins by transferring an acetyl group from acetyl-CoA to form ε-N-acetyllysine.